ID G3YC35_ASPNA Unreviewed; 2152 AA.
AC G3YC35;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Adenylate cyclase {ECO:0000256|ARBA:ARBA00021420};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
DE AltName: Full=ATP pyrophosphate-lyase {ECO:0000256|ARBA:ARBA00032597};
DE AltName: Full=Adenylyl cyclase {ECO:0000256|ARBA:ARBA00032637};
GN ORFNames=ASPNIDRAFT_178015 {ECO:0000313|EMBL:EHA19383.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA19383.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA19383.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
CC -!- FUNCTION: Plays essential roles in regulation of cellular metabolism by
CC catalyzing the synthesis of a second messenger, cAMP.
CC {ECO:0000256|ARBA:ARBA00003896}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHA19383.1}.
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DR EMBL; ACJE01000019; EHA19383.1; -; Genomic_DNA.
DR STRING; 380704.G3YC35; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1223346; -.
DR HOGENOM; CLU_000430_4_0_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd00143; PP2Cc; 1.
DR CDD; cd17214; RA_CYR1_like; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR013716; Adenylate_cyclase_G-a-bd.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR000159; RA_dom.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR Pfam; PF08509; Ad_cyc_g-alpha; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00789; Ad_cyc_g-alpha; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 9.
DR SMART; SM00365; LRR_SD22; 4.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 2.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50200; RA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 612..703
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1401..1679
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1737..1874
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2113..2152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2113..2139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2152 AA; 239220 MW; 91D80AB250109A85 CRC64;
MSHRNSDQSG GRRSSESSGA HSWLSQETVR EGRSHQPQHN HEPSNARSVS PLSGFRDTDR
PDPQTCASPT IKDPNDLYSS IFSWGSDFAP KDQRKPPQFG SHRKAMNLLG TEDPGTSPTA
NLNNRPPQLN LNPPDNSHQD AEPSLASSPT MAPNDGPSTF FNDYSEQEAS PASNLFRPGT
AQTYASEPLE LDYNGDHRRP SVASAMTVSS QGSKSSAGAL FKKKLQGFFG DEYVGNGEPR
HDSDNFTQNS ATKPSSLDQF RARERANSDG SRNPGASPAP NQARPHTPLP SSEITPWLYQ
SFNDIPQYGE APVREAPTMT ADGQRGSVSQ RDQSRRHFSG HRHSRSKEEK PTVAGDLAGY
SNRPATGRDD LSLGLRPSRE GSLNYPTPMT STTTLVGRST SPTPSVQSAY SREQGQNSPG
AQTSKRSFLD KIRRPKHGHL KNITGSKAVQ ETTKAAASKL SRREASPARR GRQGSIESGT
SSRLADSGDN ERKRDGKGLA IGSAKLRGRR GHGNEVPPGK DTRQPDRSNV WELDTDLSHM
EGIVNPPSPS AKSKMFDGAS IRSEETRRRD AVPAGNWDAP ESWHVKKQNE PSTLLPQDTS
EPGPTITEPD GPNWYIRIFR PDATFATLSG GLYATVADLV HGLSRKSFLT EHISNYELVM
QKNDLSRQLD QTEMPILMQK RMLEQVGYTE KDRIEEVGRE DHSYILRFTF LPARITGYII
DGNDPLGKAQ QKFSHVDLSN RCLVTIPIGL YKKAPEIISL NLSKNLALDV PKDFIQGCIN
LREIKFIGNE ALRLPASFGL ASRLTYLDVS NNFLEDLTHA NLDRLHGLVS IKMANNRLTK
LPSYFGNFQY LRSLNISSNN FKVFPDLLCG LKSLVDLDIS FNNISELPQI GKLATLERIW
MTNNIVRGAL DDTFRDLVNL KEIDARFNEI TNIDTLCVLP RLEQVAIGHN AISKFKGSFP
KLRTLALDHC PMTQFEIDAP MPTLTSLNIA SAKLVQLRDT FFENLPNLTK VILDKNHFVS
MSPHIGKLRK LEHFSMIKNP LAALPATIGC LTELKYLNLR ECNLRRLPPE IWHCLRLETL
NVSSNVLEGF PKHGSPQPQV PSEPIGTPAA TPGVSTTPSY EELGALEEQE ARRPSQTSGG
VLSTGSSPNG GAYRKPSVAS SLGQGRKVSA ASRSLTDGSP SSRKDSNFSQ HVATTFGGSL
RNLYLADNRL EDDIFRELSL IPELRIVNLS YNELTELPQG LLRRWPLLTE LYISGNELTS
LPSDDLEEGS SLRVLHINAN RFQVLPAELC KVSKLSILDV GSNSLKYNVS NWPYDWNWNW
NRNLKYLNFS GNKRLEIKPP GSSLSNQQQQ PKHQTNLTDF TSLTHLRVLG LMDVTLTITT
IPEENEDRRV RTSASLAGSL AYGMADFLGK SEHLSIFDMI VPRLKPDKVE TVVGMFDGQS
QSSGGSRIAK FLHENFIHTF SSELKRMRPE QHETPLDALR RAFLTLNKNM AFACYKSLDQ
DVRQYQEDPT DQRRVRLTKD DIDLGGVATV MYLNNMDLYV ANVGDAQAIL VKADGSLRHL
TQNHDPAETH ERARIRDAGG FVSRTGKLND VLTVSRAFGH FPMMPAVIAA PHTMHVNLTE
QDEMVILASR ELWDYVTPDL VVDVTRAERR DLMIAAQKIR DLAISFGATN KLMVMILGVG
NLKRREKIRT RPSLSMVGPP EEQIIPSTKR TKKPRDAPGD SRLARFNYVD APVGELAIIF
TDIKKSTSLW ETCPDAMRSA IQIHNDILRR QLGIIGGYEV KTEGDAFMVA FSTTTAALLW
CFNCQTQLLD AEWPTEILEQ PQCQVVYDTE NNIIFRGLSV RMGSHWGEPV CEKDPVTNRM
DYFGPMVNRA SRISAVADGG QIFVSSDFMS DIQRNLEIFA DSERAASTGS EESYALDTLG
HNIRRELQQL NSQGFVIKDQ GERKLKGLEN PEPLYLIYPH GLSGRLTTLD KDASNELAPT
TISKHSQLEI QTDLIWRLWE ITLRLERLCA ALEYPGEARL KEPNVALFNV VKNHGGELAD
STVISLVEQQ VTRIEVCITT LFIRNMMRPF RPGDQLNDHA VPITDVMQQL QAQLAEFRAL
KEQIDASAGT ATSYTYTDPQ YSNGESNYDS ASSSYLHMGP PSDEFNPGGP RP
//
